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- W2030504047 abstract "Syntrophins are known to self-associate to form oligomers. Mouse α1-syntrophin sequences were produced as chimeric fusion proteins in bacteria and were found to also oligomerize and in a micromolar Ca2+-dependent manner. The oligomerization was localized to the N-terminal pleckstrin homology domain (PH1) or adjacent sequences; the second, C-terminal PH2 domain did not show oligomerization. PH1 was found to self-associate, and calmodulin or Ca2+-chelating agents such as ethylene glycol bis(β-aminoethyl ether)-N,N,N‘,N‘-tetraacetic acid (EGTA) could effectively prevent this oligomerization. A single calmodulin bound per syntrophin to cause inhibition of the precipitation. Since calmodulin inhibited syntrophin oligomerization in the presence or absence of Ca2+, Ca2+ binding to syntrophin is responsible for the inhibition by EGTA of syntrophin oligomerization." @default.
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- W2030504047 date "2000-08-01" @default.
- W2030504047 modified "2023-09-25" @default.
- W2030504047 title "Oligomerization of Mouse α1-Syntrophin and Self-Association of Its Pleckstrin Homology Domain 1 Containing Sequences†" @default.
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- W2030504047 doi "https://doi.org/10.1021/bi0000824" @default.
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